Peptide sequence determination by matrix-assisted laser desorption ionization employing a tandem double focusing magnetic—Orthogonal acceleration time-of-flight mass spectrometer View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1996-01-01

AUTHORS

Katalin F. Medzihradszky, Gregory W. Adams, Alma L. Burlingame, Robert H. Bateman, Martin R. Green

ABSTRACT

This report describes the fragmentation processes for peptides induced by collisional activation of the 12C isobar of matrix-assisted laser desorption ionization (MALDI)-generated pseudomolecular ions employing an EBE orthogonal acceleration time-of-flight mass spectrometer and using xenon as the collision gas at a laboratory collision energy of 800 eV. These MALDI-collision-induced dissociation (CID) spectra are shown to provide sequence information of comparable quality to those obtained by using high energy CID conditions with liquid secondary ionization mass spectrometry on a four-sector tandem instrument. Peptide sequencing via MALDI-CID is demonstrated on three tryptic peptides obtained from a bacterial protein (P450 isozyme) of unknown sequence. Sensitivity is shown to be at the 1 pmol level for standard peptides. More... »

PAGES

1-10

Identifiers

URI

http://scigraph.springernature.com/pub.10.1016/1044-0305(95)00621-4

DOI

http://dx.doi.org/10.1016/1044-0305(95)00621-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1039547150

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24202789


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